ID GLT12_HUMAN Reviewed; 581 AA. AC Q8IXK2; Q5TCF7; Q8NG54; Q96CT9; Q9H771; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 3. DT 27-MAR-2024, entry version 184. DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 12; DE EC=2.4.1.41; DE AltName: Full=Polypeptide GalNAc transferase 12; DE Short=GalNAc-T12; DE Short=pp-GaNTase 12; DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 12; DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12; GN Name=GALNT12; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, TISSUE RP SPECIFICITY, AND VARIANT VAL-119. RC TISSUE=Lung; RX PubMed=12135769; DOI=10.1016/s0014-5793(02)03007-7; RA Guo J.-M., Zhang Y., Cheng L., Iwasaki H., Wang H., Kubota T., RA Tachibana K., Narimatsu H.; RT "Molecular cloning and characterization of a novel member of the UDP- RT GalNAc:polypeptide N-acetylgalactosaminyltransferase family, pp-GalNAc- RT T12(1)."; RL FEBS Lett. 524:211-218(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Bennett E.P.; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Bone marrow; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-581 (ISOFORM 1). RC TISSUE=Colon; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP VARIANTS CRCS1 TRP-297; ASN-303; ASP-341; HIS-373; HIS-382; PHE-479 AND RP MET-491, CHARACTERIZATION OF VARIANTS CRCS1 TRP-297; ASN-303; ASP-341; RP HIS-373; HIS-382; PHE-479 AND MET-491, AND VARIANTS GLU-3; ARG-46; VAL-119; RP ASN-261; ARG-272 AND LYS-552. RX PubMed=19617566; DOI=10.1073/pnas.0901454106; RA Guda K., Moinova H., He J., Jamison O., Ravi L., Natale L., Lutterbaugh J., RA Lawrence E., Lewis S., Willson J.K., Lowe J.B., Wiesner G.L., RA Parmigiani G., Barnholtz-Sloan J., Dawson D.W., Velculescu V.E., RA Kinzler K.W., Papadopoulos N., Vogelstein B., Willis J., Gerken T.A., RA Markowitz S.D.; RT "Inactivating germ-line and somatic mutations in polypeptide N- RT acetylgalactosaminyltransferase 12 in human colon cancers."; RL Proc. Natl. Acad. Sci. U.S.A. 106:12921-12925(2009). RN [7] RP VARIANTS CRCS1 ASN-303 AND CYS-396. RX PubMed=22461326; DOI=10.1002/humu.22088; RA Clarke E., Green R.C., Green J.S., Mahoney K., Parfrey P.S., RA Younghusband H.B., Woods M.O.; RT "Inherited deleterious variants in GALNT12 are associated with CRC RT susceptibility."; RL Hum. Mutat. 33:1056-1058(2012). RN [8] RP INVOLVEMENT IN CRCS1. RX PubMed=24115450; DOI=10.1002/humu.22454; RA Segui N., Pineda M., Navarro M., Lazaro C., Brunet J., Infante M., RA Duran M., Soto J.L., Blanco I., Capella G., Valle L.; RT "GALNT12 is not a major contributor of familial colorectal cancer type X."; RL Hum. Mutat. 35:50-52(2014). CC -!- FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide CC biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a CC serine or threonine residue on the protein receptor. Has activity CC toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no CC detectable activity with Muc2 and Muc7. Displays enzymatic activity CC toward the Gal-NAc-Muc5AC glycopeptide, but no detectable activity to CC mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. May play an CC important role in the initial step of mucin-type oligosaccharide CC biosynthesis in digestive organs. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O- CC [N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP; CC Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41; CC Evidence={ECO:0000269|PubMed:12135769}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3- CC O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) + CC UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41; CC Evidence={ECO:0000269|PubMed:12135769}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single- CC pass type II membrane protein {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8IXK2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8IXK2-2; Sequence=VSP_011217; CC -!- TISSUE SPECIFICITY: Widely expressed at different levels of expression. CC Highly expressed in digestive organs such as small intestine, stomach, CC pancreas and colon. Expressed at intermediate level in testis, thyroid CC gland and spleen. Weakly expressed in whole brain, cerebral cortex, CC cerebellum, fetal brain, bone marrow, thymus, leukocytes, heart, CC skeletal muscle, liver, lung, esophagus, kidney, adrenal gland, mammary CC gland, uterus, placenta, ovary and prostate. CC {ECO:0000269|PubMed:12135769}. CC -!- DOMAIN: There are two conserved domains in the glycosyltransferase CC region: the N-terminal domain (domain A, also called GT1 motif), which CC is probably involved in manganese coordination and substrate binding CC and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), CC which is probably involved in catalytic reaction and UDP-Gal binding. CC {ECO:0000250}. CC -!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes CC to the glycopeptide specificity. {ECO:0000250}. CC -!- DISEASE: Colorectal cancer 1 (CRCS1) [MIM:608812]: A complex disease CC characterized by malignant lesions arising from the inner wall of the CC large intestine (the colon) and the rectum. Genetic alterations are CC often associated with progression from premalignant lesion (adenoma) to CC invasive adenocarcinoma. Risk factors for cancer of the colon and CC rectum include colon polyps, long-standing ulcerative colitis, and CC genetic family history. {ECO:0000269|PubMed:19617566, CC ECO:0000269|PubMed:22461326, ECO:0000269|PubMed:24115450}. Note=Disease CC susceptibility is associated with variants affecting the gene CC represented in this entry. The role of GALNT12 in colon cancer CC susceptibility is however subject to discussion: studies on 103 CC probants with colorectal cancer 1 (CRCS1) suggest that it does not act CC as a major contributor of CRCS1 (PubMed:24115450). CC {ECO:0000269|PubMed:24115450}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T CC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15027.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; CC Note=Polypeptide N-acetylgalactosaminyltransferase 12; CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_495"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB078146; BAC07181.1; -; mRNA. DR EMBL; AJ132365; CAC80100.2; -; mRNA. DR EMBL; AL136084; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC013945; AAH13945.1; -; mRNA. DR EMBL; AK024865; BAB15027.1; ALT_INIT; mRNA. DR CCDS; CCDS6737.1; -. [Q8IXK2-1] DR RefSeq; NP_078918.3; NM_024642.4. [Q8IXK2-1] DR RefSeq; XP_006717350.1; XM_006717287.1. DR PDB; 6PXU; X-ray; 2.01 A; A/B=39-581. DR PDBsum; 6PXU; -. DR AlphaFoldDB; Q8IXK2; -. DR SMR; Q8IXK2; -. DR BioGRID; 122816; 120. DR IntAct; Q8IXK2; 33. DR MINT; Q8IXK2; -. DR STRING; 9606.ENSP00000364150; -. DR CAZy; CBM13; Carbohydrate-Binding Module Family 13. DR CAZy; GT27; Glycosyltransferase Family 27. DR UniLectin; Q8IXK2; -. DR GlyGen; Q8IXK2; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q8IXK2; -. DR PhosphoSitePlus; Q8IXK2; -. DR SwissPalm; Q8IXK2; -. DR BioMuta; GALNT12; -. DR DMDM; 84028209; -. DR EPD; Q8IXK2; -. DR jPOST; Q8IXK2; -. DR MassIVE; Q8IXK2; -. DR MaxQB; Q8IXK2; -. DR PaxDb; 9606-ENSP00000364150; -. DR PeptideAtlas; Q8IXK2; -. DR ProteomicsDB; 71019; -. [Q8IXK2-1] DR ProteomicsDB; 71020; -. [Q8IXK2-2] DR Pumba; Q8IXK2; -. DR Antibodypedia; 29005; 106 antibodies from 15 providers. DR DNASU; 79695; -. DR Ensembl; ENST00000375011.4; ENSP00000364150.3; ENSG00000119514.7. [Q8IXK2-1] DR GeneID; 79695; -. DR KEGG; hsa:79695; -. DR MANE-Select; ENST00000375011.4; ENSP00000364150.3; NM_024642.5; NP_078918.3. DR UCSC; uc004ayz.3; human. [Q8IXK2-1] DR AGR; HGNC:19877; -. DR CTD; 79695; -. DR DisGeNET; 79695; -. DR GeneCards; GALNT12; -. DR HGNC; HGNC:19877; GALNT12. DR HPA; ENSG00000119514; Tissue enhanced (epididymis, intestine, stomach). DR MalaCards; GALNT12; -. DR MIM; 608812; phenotype. DR MIM; 610290; gene. DR neXtProt; NX_Q8IXK2; -. DR OpenTargets; ENSG00000119514; -. DR PharmGKB; PA134929192; -. DR VEuPathDB; HostDB:ENSG00000119514; -. DR eggNOG; KOG3736; Eukaryota. DR GeneTree; ENSGT00940000157173; -. DR HOGENOM; CLU_013477_0_3_1; -. DR InParanoid; Q8IXK2; -. DR OMA; FSIDRAF; -. DR OrthoDB; 202750at2759; -. DR PhylomeDB; Q8IXK2; -. DR TreeFam; TF352660; -. DR BRENDA; 2.4.1.41; 2681. DR PathwayCommons; Q8IXK2; -. DR Reactome; R-HSA-5083636; Defective GALNT12 causes CRCS1. DR Reactome; R-HSA-913709; O-linked glycosylation of mucins. DR SignaLink; Q8IXK2; -. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 79695; 10 hits in 1155 CRISPR screens. DR ChiTaRS; GALNT12; human. DR GenomeRNAi; 79695; -. DR Pharos; Q8IXK2; Tbio. DR PRO; PR:Q8IXK2; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q8IXK2; Protein. DR Bgee; ENSG00000119514; Expressed in palpebral conjunctiva and 153 other cell types or tissues. DR ExpressionAtlas; Q8IXK2; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IBA:GO_Central. DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome. DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central. DR CDD; cd02510; pp-GalNAc-T; 1. DR CDD; cd00161; RICIN; 1. DR Gene3D; 2.80.10.50; -; 1. DR InterPro; IPR045885; GalNAc-T. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR035992; Ricin_B-like_lectins. DR InterPro; IPR000772; Ricin_B_lectin. DR PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1. DR PANTHER; PTHR11675:SF18; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 12; 1. DR Pfam; PF00535; Glycos_transf_2; 1. DR Pfam; PF00652; Ricin_B_lectin; 1. DR SMART; SM00458; RICIN; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. DR SUPFAM; SSF50370; Ricin B-like lectins; 1. DR PROSITE; PS50231; RICIN_B_LECTIN; 1. DR Genevisible; Q8IXK2; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Disease variant; Disulfide bond; KW Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane; KW Metal-binding; Reference proteome; Signal-anchor; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1..581 FT /note="Polypeptide N-acetylgalactosaminyltransferase 12" FT /id="PRO_0000059128" FT TOPO_DOM 1..19 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 20..37 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 38..581 FT /note="Lumenal" FT /evidence="ECO:0000255" FT DOMAIN 445..577 FT /note="Ricin B-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT REGION 43..67 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 135..244 FT /note="Catalytic subdomain A" FT REGION 304..366 FT /note="Catalytic subdomain B" FT COMPBIAS 51..67 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 176 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 205 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 228 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250" FT BINDING 230 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250" FT BINDING 335 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 363 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250" FT BINDING 371 FT /ligand="substrate" FT /evidence="ECO:0000250" FT DISULFID 125..358 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT DISULFID 349..422 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT DISULFID 458..479 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT DISULFID 506..521 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT DISULFID 547..566 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT VAR_SEQ 1..309 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_011217" FT VARIANT 3 FT /note="G -> E (in dbSNP:rs1356894484)" FT /evidence="ECO:0000269|PubMed:19617566" FT /id="VAR_064352" FT VARIANT 46 FT /note="G -> R (in dbSNP:rs10987768)" FT /evidence="ECO:0000269|PubMed:19617566" FT /id="VAR_064353" FT VARIANT 119 FT /note="E -> V (in dbSNP:rs1137654)" FT /evidence="ECO:0000269|PubMed:12135769, FT ECO:0000269|PubMed:19617566" FT /id="VAR_064354" FT VARIANT 261 FT /note="D -> N (in dbSNP:rs41306504)" FT /evidence="ECO:0000269|PubMed:19617566" FT /id="VAR_064355" FT VARIANT 272 FT /note="G -> R (in dbSNP:rs367645298)" FT /evidence="ECO:0000269|PubMed:19617566" FT /id="VAR_064356" FT VARIANT 297 FT /note="R -> W (in CRCS1; germline mutation; partial loss of FT activity; dbSNP:rs149726976)" FT /evidence="ECO:0000269|PubMed:19617566" FT /id="VAR_064357" FT VARIANT 303 FT /note="D -> N (in CRCS1; germline mutation; reduction of FT activity; dbSNP:rs145236923)" FT /evidence="ECO:0000269|PubMed:19617566, FT ECO:0000269|PubMed:22461326" FT /id="VAR_064358" FT VARIANT 341 FT /note="E -> D (in CRCS1; somatic mutation; loss of FT activity)" FT /evidence="ECO:0000269|PubMed:19617566" FT /id="VAR_064359" FT VARIANT 373 FT /note="R -> H (in CRCS1; germline mutation; partial loss of FT activity; dbSNP:rs920049418)" FT /evidence="ECO:0000269|PubMed:19617566" FT /id="VAR_064360" FT VARIANT 382 FT /note="R -> H (in CRCS1; germline mutation; loss of FT activity; dbSNP:rs868590153)" FT /evidence="ECO:0000269|PubMed:19617566" FT /id="VAR_064361" FT VARIANT 396 FT /note="Y -> C (in CRCS1; dbSNP:rs1272530441)" FT /evidence="ECO:0000269|PubMed:22461326" FT /id="VAR_068509" FT VARIANT 479 FT /note="C -> F (in CRCS1; somatic mutation; loss of FT activity)" FT /evidence="ECO:0000269|PubMed:19617566" FT /id="VAR_064362" FT VARIANT 491 FT /note="T -> M (in CRCS1; germline mutation; loss of FT activity; dbSNP:rs267606840)" FT /evidence="ECO:0000269|PubMed:19617566" FT /id="VAR_064363" FT VARIANT 552 FT /note="R -> K (in dbSNP:rs1285871027)" FT /evidence="ECO:0000269|PubMed:19617566" FT /id="VAR_064364" FT STRAND 61..65 FT /evidence="ECO:0007829|PDB:6PXU" FT TURN 75..78 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 88..101 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 105..108 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 123..127 FT /evidence="ECO:0007829|PDB:6PXU" FT TURN 132..134 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 138..146 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 149..162 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 168..175 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 181..183 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 185..191 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 197..201 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 207..218 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 221..226 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 229..233 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 238..247 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 251..260 FT /evidence="ECO:0007829|PDB:6PXU" FT TURN 262..264 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 276..279 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 285..288 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 292..297 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 315..318 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 319..324 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 334..337 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 338..348 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 352..364 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 376..387 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 389..391 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 392..398 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 400..404 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 411..419 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 425..431 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 445..454 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 457..460 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 464..467 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 475..478 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 484..486 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 488..490 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 496..498 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 500..503 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 505..508 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 517..520 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 527..529 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 531..533 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 537..541 FT /evidence="ECO:0007829|PDB:6PXU" FT TURN 542..545 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 546..551 FT /evidence="ECO:0007829|PDB:6PXU" FT TURN 554..556 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 560..564 FT /evidence="ECO:0007829|PDB:6PXU" FT HELIX 570..572 FT /evidence="ECO:0007829|PDB:6PXU" FT STRAND 573..579 FT /evidence="ECO:0007829|PDB:6PXU" SQ SEQUENCE 581 AA; 66938 MW; 8C001D58E103A523 CRC64; MWGRTARRRC PRELRRGREA LLVLLALLAL AGLGSVLRAQ RGAGAGAAEP GPPRTPRPGR REPVMPRPPV PANALGARGE AVRLQLQGEE LRLQEESVRL HQINIYLSDR ISLHRRLPER WNPLCKEKKY DYDNLPRTSV IIAFYNEAWS TLLRTVYSVL ETSPDILLEE VILVDDYSDR EHLKERLANE LSGLPKVRLI RANKREGLVR ARLLGASAAR GDVLTFLDCH CECHEGWLEP LLQRIHEEES AVVCPVIDVI DWNTFEYLGN SGEPQIGGFD WRLVFTWHTV PERERIRMQS PVDVIRSPTM AGGLFAVSKK YFEYLGSYDT GMEVWGGENL EFSFRIWQCG GVLETHPCSH VGHVFPKQAP YSRNKALANS VRAAEVWMDE FKELYYHRNP RARLEPFGDV TERKQLRDKL QCKDFKWFLE TVYPELHVPE DRPGFFGMLQ NKGLTDYCFD YNPPDENQIV GHQVILYLCH GMGQNQFFEY TSQKEIRYNT HQPEGCIAVE AGMDTLIMHL CEETAPENQK FILQEDGSLF HEQSKKCVQA ARKESSDSFV PLLRDCTNSD HQKWFFKERM L //